1ctn: Difference between revisions
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[[Image:1ctn.gif|left|200px]] | [[Image:1ctn.gif|left|200px]] | ||
'''CRYSTAL STRUCTURE OF A BACTERIAL CHITINASE AT 2.3 ANGSTROMS RESOLUTION''' | {{Structure | ||
|PDB= 1ctn |SIZE=350|CAPTION= <scene name='initialview01'>1ctn</scene>, resolution 2.3Å | |||
|SITE= | |||
|LIGAND= | |||
|ACTIVITY= [http://en.wikipedia.org/wiki/Chitinase Chitinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.14 3.2.1.14] | |||
|GENE= | |||
}} | |||
'''CRYSTAL STRUCTURE OF A BACTERIAL CHITINASE AT 2.3 ANGSTROMS RESOLUTION''' | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
1CTN is a [ | 1CTN is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Serratia_marcescens Serratia marcescens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1CTN OCA]. | ||
==Reference== | ==Reference== | ||
Crystal structure of a bacterial chitinase at 2.3 A resolution., Perrakis A, Tews I, Dauter Z, Oppenheim AB, Chet I, Wilson KS, Vorgias CE, Structure. 1994 Dec 15;2(12):1169-80. PMID:[http:// | Crystal structure of a bacterial chitinase at 2.3 A resolution., Perrakis A, Tews I, Dauter Z, Oppenheim AB, Chet I, Wilson KS, Vorgias CE, Structure. 1994 Dec 15;2(12):1169-80. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/7704527 7704527] | ||
[[Category: Chitinase]] | [[Category: Chitinase]] | ||
[[Category: Serratia marcescens]] | [[Category: Serratia marcescens]] | ||
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[[Category: lyase (oxo-acid)]] | [[Category: lyase (oxo-acid)]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 10:28:43 2008'' | ||
Revision as of 11:28, 20 March 2008
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| , resolution 2.3Å | |||||||
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| Activity: | Chitinase, with EC number 3.2.1.14 | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
CRYSTAL STRUCTURE OF A BACTERIAL CHITINASE AT 2.3 ANGSTROMS RESOLUTION
OverviewOverview
BACKGROUND: Chitinases cleave the beta-1-4-glycosidic bond between the N-acetyl-D-glucosamine units of which chitin is comprised. Chitinases are present in plants, bacteria and fungi, but whereas structures are available for two prototypic plant enzymes, no structure is available for a bacterial or fungal chitinase. RESULTS: To redress this imbalance, the structure of native chitinase A from Serratia marcescens has been solved by multiple isomorphous replacement and refined at 2.3 A resolution, resulting in a crystallographic R-factor of 16.2%. The enzyme comprises three domains: an all beta-strand amino-terminal domain, a catalytic alpha/beta-barrel domain, and a small alpha+beta-fold domain. There are several residues with unusual geometries in the structure. Structure determination of chitinase A in complex with N,N',N",N"'-tetra-acetylo-chitotetraose, together with biochemical and sequence analysis data, enabled the positions of the active-site and catalytic residues to be proposed. CONCLUSIONS: The reaction mechanism seems to be similar to that of lysozyme and most other glycosylhydrolases, i.e. general acid-base catalysis. The role of the amino-terminal domain could not be identified, but it has similarities to the fibronectin III domain. This domain may possibly facilitate the interaction of chitinase A with chitin.
About this StructureAbout this Structure
1CTN is a Single protein structure of sequence from Serratia marcescens. Full crystallographic information is available from OCA.
ReferenceReference
Crystal structure of a bacterial chitinase at 2.3 A resolution., Perrakis A, Tews I, Dauter Z, Oppenheim AB, Chet I, Wilson KS, Vorgias CE, Structure. 1994 Dec 15;2(12):1169-80. PMID:7704527
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